EP2611898A1 - Konzentriertes einweichwaschverfahren - Google Patents

Konzentriertes einweichwaschverfahren

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Publication number
EP2611898A1
EP2611898A1 EP11751856.3A EP11751856A EP2611898A1 EP 2611898 A1 EP2611898 A1 EP 2611898A1 EP 11751856 A EP11751856 A EP 11751856A EP 2611898 A1 EP2611898 A1 EP 2611898A1
Authority
EP
European Patent Office
Prior art keywords
wash
detergent
enzymes
column
enzyme
Prior art date
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
Withdrawn
Application number
EP11751856.3A
Other languages
English (en)
French (fr)
Inventor
Lilian Eva Tang Baltsen
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Novozymes AS
Original Assignee
Novozymes AS
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Application filed by Novozymes AS filed Critical Novozymes AS
Priority to EP11751856.3A priority Critical patent/EP2611898A1/de
Publication of EP2611898A1 publication Critical patent/EP2611898A1/de
Withdrawn legal-status Critical Current

Links

Classifications

    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D11/00—Special methods for preparing compositions containing mixtures of detergents ; Methods for using cleaning compositions
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/38—Products with no well-defined composition, e.g. natural products
    • C11D3/386—Preparations containing enzymes, e.g. protease or amylase
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/38—Products with no well-defined composition, e.g. natural products
    • C11D3/386—Preparations containing enzymes, e.g. protease or amylase
    • C11D3/38618—Protease or amylase in liquid compositions only
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/38—Products with no well-defined composition, e.g. natural products
    • C11D3/386—Preparations containing enzymes, e.g. protease or amylase
    • C11D3/38627—Preparations containing enzymes, e.g. protease or amylase containing lipase
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/38—Products with no well-defined composition, e.g. natural products
    • C11D3/386—Preparations containing enzymes, e.g. protease or amylase
    • C11D3/38636—Preparations containing enzymes, e.g. protease or amylase containing enzymes other than protease, amylase, lipase, cellulase, oxidase or reductase
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/38—Products with no well-defined composition, e.g. natural products
    • C11D3/386—Preparations containing enzymes, e.g. protease or amylase
    • C11D3/38645—Preparations containing enzymes, e.g. protease or amylase containing cellulase
    • D—TEXTILES; PAPER
    • D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
    • D06F—LAUNDERING, DRYING, IRONING, PRESSING OR FOLDING TEXTILE ARTICLES
    • D06F13/00—Washing machines having receptacles, stationary for washing purposes, with agitators therein contacting the articles being washed 
    • C11D2111/12—
    • C11D2111/44—

Definitions

  • the present invention relates to wash processes for cold water wash.
  • the invention relates to concentrated liquid soak wash processes comprising at least one enzyme and at least one surfactant.
  • WO07/008776 relates to a single-dose enzyme tablet for enhancing and/or supplementing the performance of commercially available fabric and dish care products and providing a cleaning benefit. Such benefit is achieved when using a regular or normal wash temperature and a conventional wash cycle time, the wash performance is improved.
  • WO08/101958 relates to a method for laundering fabrics, wherein a foam composition comprising enzymes is distributed over fabrics. After a holding period, water and optionally a detergent composition are added and the fabrics are washed under usual washing conditions.
  • US2008/0276972 relates to a wash cycle for oxidizing agents wherein a first and subsequently a second wash liquor is dispensed into a wash zone.
  • the wash liquors being either detergent wash liquor or oxidizing wash liquor.
  • the inventors have developed a wash process comprising an initial concentrated surfactant and enzyme soak followed by a main wash and surprisingly found that this concentrated liquid soak wash process shows a significant increase in stain removal on a very broad range of stains and an improved wash performance in general.
  • the use of selected chemistry for detergent compositions in combination with a changed wash process has shown to improve the wash performance for a range of temperatures and in particular at low or cold temperatures.
  • the cleaning efficiency for cold concentrated soak wash processes has been increased to a level that matches the currently used warm wash process.
  • the amount of chemicals used may be increased with a simultaneous increase in wash performance.
  • the cost-benefit balance may no longer be favorable or a plateau may even be reached where further stain removal is not observed, or the detergency is even reduced. It would therefore be desirable to optimize the use of the chemicals added.
  • the concentrated soak wash process raises this upper limit and opens for a better wash performance in particular at cold wash conditions.
  • currently used chemistry such as commercially available detergents that are formulated with as well as without enzymes may be used and result in increased wash performance.
  • the invention in a first aspect relates to a method for cleaning an object comprising the steps: (a) distributing to the object a first soak solution comprising at least one surfactant and at least one enzyme followed by a first soak period wherein the concentrations of the at least one surfactant and the at least one enzyme are higher relative to their concentrations in a subsequent wash solution; (b) furthermore adding to the object water to obtain a wash solution followed by a wash period; and (c) rinsing the object; wherein said method has a wash performance corresponding to any of (i) a Relative Wash Performance (RWP) of at least 1 ; (ii) a Process Related Cleaning Index (PRCI) of more than 1 ; or (iii) a Relative Wash Performance (RWP) of at least 1 and a Process Related Cleaning Index (PRCI) of more than 1.
  • RWP Relative Wash Performance
  • PRCI Process Related Cleaning Index
  • PRCI Process Related Cleaning Index
  • the invention relates to use of the method for cleaning laundry.
  • the invention relates to a novel wash process which in comparison with a normal wash process has improved wash performance and at the same time provides means for washing at low and/or cold temperatures and for using less detergent and water whereby the overall energy consumption can be reduced.
  • the wash process not only shows an improved cleaning effect in comparison with a normal wash conducted at the same temperature but surprisingly demonstrates an overall wash performance when conducted at 20°C that match the level of a "normal heavy duty wash” at 40°C. This effect is observed even on stains that normally changes physical state at reduced or cold temperatures such as lard and sebum and other fatty material that harden and crystallize at cold conditions and melt at warmer (40°C and above) conditions.
  • the concentrated liquid soak wash process is characterized by reduced energy consumption as compared to a normal wash process due to the improved detergency power at low temperature.
  • the energy for heating wash water is by far the most energy consuming part of the wash process. Due to the concentrated soak period in which the period with agitation or other mechanical action is low the overall wash time may be cut, the total water consumption is decreased and there is less mechanical wear of the object.
  • Benchmark The terms "Benchmark” or “Benchmark cleaning” in relation to a process of the invention are defined herein as both denoting the cleaning performance resulting from using the same detergent/wash solution as used in the process in question in a normal wash at the same temperature. It is expressed as a delta remission value (see definition below). In the examples the results relating to the benchmark are in most cases shown in column a.
  • Concentrated soak wash process The terms “Concentrated soak wash”, “Concentrated soak-wash process”, “2-stage wash process” and “liquid concentrated soak wash” are defined herein as synonyms.
  • liquid may be included such as in “liquid concentrated soak wash” to emphasize that soaking is performed by applying to the object a solution and not non-liquid compositions such as foam.
  • Delta remission value (ARem): The terms "Delta remission” or “Delta remission value” are defined herein as the result of a reflectance or remission measurement at 460 nm.
  • the swatch is measured with one swatch of similar color as background, preferably a swatch from a repetition wash. A swatch representing each swatch type is measured before wash.
  • the Delta remission is the remission value of the washed swatch minus the remission value of the unwashed swatch.
  • Normal wash process The terms "Normal wash” or “Normal wash process” are defined herein as a one-step wash process wherein the object is cleaned by submerging the object in a wash solution during agitation followed by rinsing.
  • Process-related Cleaning Index (at a given temperature) is defined herein as the cleaning performance of the wash process according to the invention at that temperature relative to the cleaning performance of the benchmark.
  • Relative Wash Performance is defined herein as the wash performance of the wash process according to the invention conducted at a given temperature (X°C) relative to the wash performance of a normal wash process at 40°C using the same detergent ingredients at the same levels in the wash solution.
  • the present invention relates to a method for cleaning an object comprising the steps: (a) distributing to the object a first soak solution comprising at least one surfactant and at least one enzyme followed by a first soak period wherein the concentrations of the at least one surfactant and the at least one enzyme are higher relative to their concentrations in a subsequent wash solution; (b) furthermore adding to the object water to obtain a wash solution followed by a wash period; and (c) rinsing the object; wherein said method has a wash performance corresponding to any of (i) a Relative Wash Performance (RWP) of at least 1 ; (ii) a Process Related Cleaning Index (PRCI) of more than 1 ; or (iii) a Relative Wash Performance (RWP) of at least 1 and a Process Related Cleaning Index (PRCI) of more than 1.
  • RWP Relative Wash Performance
  • PRCI Process Related Cleaning Index
  • PRCI Process Related Cleaning Index
  • the invention relates to a method, the wherein the object is fabric/textile.
  • the wash process may be conducted manually or mechanically in a container or any suitable washing device that may accommodate the object to be cleaned and the soak and wash solutions. Soak
  • the object to be cleaned and a soak solution are added to a suitable container or washing device and in a first step the object is soaked in the soak solution.
  • the soak solution is an aqueous solution comprising at least one surfactant and at least one enzyme.
  • the at least one surfactant and the at least one enzyme may be added individually or as a mixture. They may also be added comprised in a fully formulated detergent composition.
  • the at least one enzyme may furthermore be added together with a detergent composition which detergent composition may be formulated with or without enzyme.
  • the present wash process requires that at least one enzyme is present in the soak solution. In some embodiments there may be at least two, at least three, at least four, at least five, at least six, at least seven, at least eight, at least nine or at least ten enzymes present in the soak solution. Typically a mixture of selected enzymes is used. Selection of enzyme(s) to be included in the soak solution is dependent on the type of stains to be treated.
  • the invention relates to a method, wherein the at least one enzyme is selected from the group consisting of: hemicellulases, peroxidases, proteases, cellulases, xylanases, lipases, phospholipases, esterases, cutinases, pectinases, mannanases, pectate lyases, keratinases, reductases, oxidases, phenoloxidases, lipoxygenases, ligninases, pullulanases, tannases, pentosanases, malanases, beta-glucanases, arabinosidases, hyaluronidases, chondroitinases, laccases, and amylases, or any combination thereof.
  • the at least one enzyme is selected from the group consisting of: hemicellulases, peroxidases, proteases, cellulases, xylanases, lipases, phospholipases
  • the invention relates to a method, wherein the at least one enzyme is a mixture comprising or consisting of an amylase, a cellulase, a lipase and a protease.
  • Hemicellulases are the most complex group of non-starch polysaccharides in the plant cell wall. They consist of polymers of xylose, arabinose, galactose, mannose and/or glucose which are often highly branched and connected to other cell wall structures. Hemicellulases of the present invention therefore include enzymes with xylanolytiactivity, arabinolytic activity, galactolytic activity and/or mannolytic activity.
  • the hemi-cellulases of the present invention may for example be selected from xylanases (EC3.2.1 .8, EC3.2.1.32, and EC3.2.1.136), xyloglucanases (EC3.2.1.4 and EC3.2.1 .151), arabinofuranosidases (EC3.2.1.55), acetylxylan esterases (EC3.1 .1 .72), glucuronidases (EC3.2.1 .31 , EC3.2.1 .56, EC3.2.1.128 and EC3.2.1.139), glucanohydrolase (EC3.2.1.11 , EC3.2.1.83 and EC3.2.1.73), ferulic acid esterases (EC3.1.1.73), coumaric acid esterases (EC3.1.1.73), mannanases (EC3.2.1.25; EC3.2.1 .78 and EC3.2.1.101), arabinosidase (EC3.2.1.88), arabinanases (EC3.2.1.99), gal
  • Mannananase is a preferred hemicellulase in relation to the present invention.
  • Mannanases hydrolyse the biopolymers made up of galactomannans.
  • Mannan containing stains often comprise guar gum and locust bean gum, which are widely used as stabilizers in food and cosmetic products.
  • Suitable mannanases include those of bacterial or fungal origin. Chemically or genetically modified mutants are included.
  • the mannanase is derived from a strain of the genus Bacillus, especially Bacillus sp.
  • mannanase is Mannaway ® produced by Novozymes A/S or PurabriteTM produced by Genencor a Danisco division.
  • Xylanase is a preferred hemicellulase in relation to the present invention.
  • a suitable commercially available xylanase is Pulpzyme ® HC (available from Novozymes A S).
  • pectinases The term pectinase or pectolytic enzyme is intended to include any pectinase enzyme defined according to the art where pectinases are a group of enzymes that catalyze the cleavage of glycosidic linkages. Basically three types of pectolytic enzymes exist: pectinesterase, which only removes methoxyl residues from pectin, a range of depolymerizing enzymes, and protopectinase, which solubilizes protopectin to form pectin (Sakai et al., (1993) Advances in Applied Microbiology vol.39 pp213-294).
  • pectinases or pectolytic enzyme useful in the invention is pectate lyase (EC4.2.2.2 and EC4.2.2.9), polygalacturonase (EC3.2.1.15 and EC3.2.1.67), polymethyl galacturonase, pectin lyase (EC4.2.2.10), galactanases (EC3.2.1.89), arabinanases (EC3.2.1.99) and/or pectin esterases (EC3.1.1.11).
  • Pectinaceous soils or stains may for example be composed of pectate, polygalacturonicacid, and/or pectin which may be esterified to a higher or lower degree.
  • These substrates are common in soils of vegetable origin which may include grass, vegetables such as spinach, beetroot, carrot, tomatoes, fruits such as all types of cherries and berries, peach, apricot, mango, bananas and grapes as well as stains from drinks derived from plant material, such as wine, beer, fruit juices and additionally tomato sauce, jellies or jams without excluding other pectin containing substances.
  • Suitable pectinolytic enzymes include those described in WO99/27083, WO99/27084,
  • Suitable pectate lyases include those of bacterial or fungal origin. Chemically or genetically modified mutants are included.
  • the pectate lyase is derived from a strain of the genus Bacillus, especially a strain of Bacillus substilis, especially Bacillus subtilis DSM14218 disclosed in SEQ ID NO:2 or a variant thereof disclosed in Example 6 of WO02/092741 (hereby incorporated by reference) or a variant disclosed in WO03/095638 (hereby incorporated by reference).
  • the pectate lyase is derived from a strain of Bacillus licheniformis, especially the pectate lyases disclosed as SEQ ID NO:8 in WO99/27083 (hereby incorporated by reference) or variants thereof as described in WO02/06442.
  • Suitable commercially available pectate lyases are Pectaway ® or Pectawash ® produced by Novozymes A S.
  • Amylases Common starch containing stains may for example comprise rice, potato, cereals, noodles, pasta and porridge, without excluding other starch containing substances. Starch stains may not always be visible to the naked eye but starch stains tend to act as glue for particulate soils in wash solutions. Amylases prevent the buildup of starch deposits which may cause discoloration on fabrics and starch films on dishes. Amylases comprise e.g. alpha-amylases (EC3.2.1.1), beta-amylases (EC3.2.1 .2) and/or glucoamylases (EC3.2.1.3) of bacterial or fungal origin. Chemically or genetically modified mutants of such amylases are included in this connection. Alpha-amylases are preferred in relation to the present invention. Relevant alpha-amylases include, for example, a-amylases obtainable from Bacillus species, in particular a special strain of B. licheniformis, described in more detail in GB1296839.
  • useful amylases are the variants described in WO94/02597, W094/18314, W096/23873, and W097/43424, especially the variants with substitutions in one or more of the following positions: 15, 23, 105, 106, 124, 128, 133, 154, 156, 181 , 188, 190, 197, 202, 208, 209, 243, 264, 304, 305, 391 , 408, and 444.
  • Further examples of useful amylases are the alpha- amylases derived from Bacillus sp. he AA560 alpha-amylase derived from Bacillus sp.
  • DSM 12649 disclosed as SEQ ID NO:2 in WOOO/60060 (hereby incorporated by reference) and the variants of the AA560 alpha-amylase, including the AA560 variant disclosed in Example 7 and 8 (hereby incorporated by reference).
  • amylases include Natalase ® , Stainzyme ® , Duramyl ® , Termamyl ® , TermamylTM Ultra, Fungamyl ® and BAN ® (all available from Novozymes A/S, Bagsvaerd, Denmark), and Rapidase ® and Maxamyl ® P (available from DSM, Holland) and Purastar ® , Purastar OxAm and PoweraseTM (available from Danisco A/S).
  • CGTases cyclodextrin glucanotransferases, EC 2.4.1.19
  • those obtainable from species of Bacillus, Thermoanaerobactor or Thermoanaerobacterium are useful amylases.
  • Cellulases are primarily used for textile care, such as removal or reduction of fuzz and pills from cotton fabrics, softening, colour clarification, particulate soil removal, dye transfer inhibition and anti-redeposition of soils on cotton fabrics in the wash.
  • Suitable cellulases include complete cellulases or mono-component endoglucanases of bacterial or fungal origin with anti redeposition effect. Chemically or genetically modified mutants are included.
  • the cellulase may for example be a mono-component or a mixture of mono-component endo-1 ,4- beta-glucanase often just termed endoglucanases (EC 3.2.1 .4).
  • Some xyloglucanases may also have endoglucanases activity and are also considered as suitable cellulases in the present invention.
  • Suitable cellulases are disclosed in US4,435,307, which discloses fungal cellulases produced from Humicola insolens. Especially suitable cellulases for this invention are cellulases with anti-redeposition effect.
  • Suitable mono-component endoglucanases may be obtained from one or more of the following species Exidia glandulosa, Crinipellis scabella, Fomes fomentarius, Spongipellis sp., Rhi- zophlyctis rosea, Rhizomucor pusillus, Phycomyces nitens, and Chaetostylum fresenii , Diplodia gossypina, Microsphaeropsis sp., Ulospora bilgramii, Aureobasidium sp., Macrophomina phaseolina, Ascobolus stictoides, Saccobolus dilutellus, Peziza, Penicillium verruculosum, Peni- cillium chrysogenum, and Thermomyces verrucosus, Trichoderma reesei aka Hypocrea jecorina, - Diaporthe syngenesia, Colletotnchum lagena
  • lycopersici Fusarium oxysporum ssp. passiflora, Humicola nigrescens, Humicola grisea, Fusarium oxysporum, Thielavia terrestris or Humicola insolens.
  • One preferred endoglucanase is disclosed in W096/29397 as SEQ ID NO:9 (hereby incorporated by reference) or an enzyme with at least 70% identity thereto and variants thereof as disclosed in Example 1 of WO98/12307.
  • Another preferred endoglucanase is disclosed in WO91/017243 (SEQ ID NO:2) or endoglucanases variants as disclosed in WO94/007998.
  • Endoglucanases with an anti-redeposition effect may be obtained from fungal endoglucanases lacking a carbohydrate-binding module (CBM) from a number of bacterial sources.
  • Some sources are Humicola insolens, Bacillus sp. deposited as DSM 12648, Bacillus sp. KSMS237 deposited as FERM P-16067, Panibacillus polymyxa, and Panibacillus pabuli.
  • Specific anti- redeposition endoglucanase are disclosed in W091/17244 (hereby incorporated by reference), WO04/053039 SEQ ID NO:2 (hereby incorporated by reference), JP2000210081 position 1 to 824 of SEQ ID NO: 1 (hereby incorporated by reference).
  • Xyloglucanases with an anti-redeposition effect may be obtained from a number of bacterial sources. Some sources are Bacillus licheniformis, Bacillus agaradhaerens, (WO99/02663) Panibacillus polymyxa, and Panibacillus pabuli (WO01/62903). Suitable variants of xyloglucasnes are also described in PCT/EP2009/056875. A commercially available xyloglucanase is Whitezyme ® (Novozymes A/S).
  • cellulases include Celluclast ® produced from Trichoderma reesei,
  • Lipases Lipase or a lipolytic enzyme provides improved detergency performance on soils that contain fat or oil.
  • Common fat and/or oil containing stains may for example comprise body soils (sebum), lipstick, mayonnaise, mustard, salad dressings, vegetable fat and oil, animal fat (e.g. butter and gravy), wax and mineral oil without excluding other oil and/or fat containing substances.
  • Any lipase suitable for use in alkaline solutions can be used. Suitable lipases include those of bacterial or fungal origin. Chemically or genetically modified mutants of such lipases are included in this connection.
  • the lipase may for example be triacylglycerol lipase (EC3.1.1 .3), phospholipase A2 (EC3.1.1.4), Lysophospholipase (EC3.1 .1 .5), Monoglyceride lipase (EC3.1 .1 .23), galactolipase (EC3.1.1.26), phospholipase A1 (EC3.1.1.32), Lipoprotein lipase (EC3.1.1.34).
  • useful lipases include a Humicola lanuginosa lipase, e.g. as described in EP258068 and EP305216; a Rhizomucor miehei lipase, e.g. as described in EP238023 or from H.
  • Candida lipase such as a C. antarctica lipase, e.g. the C. antarctica lipase A or B described in EP214761 ; a Pseudomonas lipase, such as one of those described in EP721981 (e.g. a lipase obtainable from a Pseudomonas sp. SD705 strain having deposit accession number FERM BP- 4772), in PCT/JP96/00426, in PCT/JP96/00454 (e.g. a P.
  • a Candida lipase such as a C. antarctica lipase, e.g. the C. antarctica lipase A or B described in EP214761
  • Pseudomonas lipase such as one of those described in EP721981 (e.g. a lipase obtainable from a Pseudomonas sp. SD70
  • solanacearum lipase in EP571982 or in W095/14783 (e.g. a P. mendocina lipase), a P. alcaligenes or P. pseudoalcaligenes lipase, e.g. as described in EP218272, a P. cepacia lipase, e.g. as described in EP331376, a P. stutzeri lipase, e.g. as disclosed in GB1372034, or a P. fluorescens lipase; a Bacillus lipase, e.g. a B. subtilis lipase (Dartois et al.
  • a preferred lipase variant is that of Humicola lanuginosa DSM 4109 as described in WO00/60063. Especially preferred are the variants disclosed in the Example in WO00/60063 with improved first wash performance i.e., T231 R+N233R;
  • Suitable commercially available lipases include Lipex ® , Lipolase ® and Lipolase Ultra ® , Lipolex ® , Lipoclean ® (available from Novozymes A/S), M1 LipaseTM and LipomaxTM (available from Genencor Inc.) and Lipase P "Amano” (available from Amano Pharmaceutical Co. Ltd.).
  • Commercially available cutinases include LumafastTM from Genencor Inc.
  • Cutinases Potentially useful types of lipolytic enzymes include cutinases (EC3.1.1.74), e.g. a cutinase derived from Pseudomonas mendocina as described in WO88/09367, or a cutinase derived from Fusarium solani pisi (described, e.g., in WO90/09446). Due to the lipolytic activity of cutinases they may be effective against the same stains as lipases. Commercially available cutinases include LumafastTM from Genencor Inc.
  • Peroxidases/Oxidases include those of plant, bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Examples of useful peroxidases include peroxidases from Coprinus, e.g. , from C. cinereus, and variants thereof as those described in W093/24618, WO95/10602, and W098/15257. Commercially available peroxidases include GuardzymeTM (Novozymes A/S).
  • proteases are used in the removal of protein containing stains such as blood, dairy products, body soils (sebum), baby formula, mud, grass, eggs and baby food. Any protease suitable for use in alkaline solutions can be used. Suitable proteases include those of animal, vegetable or microbial origin. Microbial origin is preferred. Chemically modified or protein engineered mutants are included.
  • the protease may for example be a metalloprotease (EC3.4.17 or EC3.4.24) or a serine protease (EC3.4.21), preferably an alkaline microbial protease or a trypsin- like protease.
  • alkaline proteases are subtilisins (EC3.4.21 .62), especially those derived from Bacillus, e.g., subtilisin Novo, subtilisin Carlsberg, subtilisin 309, subtilisin 147 and subtilisin 168 (described in WO89/06279).
  • trypsin-like proteases are trypsin (e.g., of porcine or bovine origin) and the Fusarium protease described in WO89/06270 and W094/25583.
  • Examples of useful proteases are the variants described in W092/19729, WO98/201 15, WO98/201 16, and WO 98/34946, especially the variants with substitutions in one or more of the following positions: 27, 36, 57, 76, 87, 97, 101 , 104, 120, 123, 167, 170, 194, 206, 218, 222, 224, 235, and 274.
  • protease enzymes include Alcalase ® , Savinase ® , Primase ® , Duralase ® , Esperase ® , and Kannase ® (Novozymes A/S), Maxatase ® , Maxacal ® , Maxapem ® , Properase ® , Purafect ® , Purafect OxP ® , FN2TM, and FN 3TM (Genencor International Inc.).
  • 0.000001 % to 10% from 0.00001 % to 5%, from 0.0001 % to 2.5%, from 0.001 % to 2%, from 0.01 % to 1.5%, or from 0.1 % to 1 % of enzyme protein by weight of the composition.
  • the invention relates to a method wherein the at least one enzyme may be used in addition to detergent compositions in accordance with the invention at an amount from 0 to 20, from 0.00001 to 10, from 0.0001 to 5, from 0.0001 to 2.5, from 0.001 to 2, from 0.01 to
  • the invention relates to a method wherein the at least one enzyme may be used in addition to detergent compositions in accordance with the invention at a concentration from 0 to 5000, from 0.001 to 100, from 0.01 to 50, or from 0.1 to 10 milligram enzyme protein per liter soak solution.
  • the invention relates to a method wherein the level of enzyme protein by weight of the composition relates to the amount of the individual added enzyme of the at least one enzyme added. In other embodiments the invention relates to a method wherein the level of enzyme protein by weight of the composition relates to the amount of all added enzymes of the at least one enzyme added ie. the total amount of added enzyme.
  • the enzyme based wash performance is the cleaning effect provided by the enzyme and it may be expressed as an Enzyme-related Cleaning Index (ERCI) as defined supra.
  • ERCI Enzyme-related Cleaning Index
  • Example 3-III shows that by adding the same amount of enzymes to the wash processes result in a higher ERCI for the wash process according to some embodiments of the invention in comparison with a normal wash process.
  • the invention relates to a method wherein the ERCI for the 2- stage process is higher than the ERCI for the corresponding normal wash process.
  • the term "corresponding" should be understood as the wash conditions should be as identical as possible such as temperature, total wash time, added detergent components etc. all except the wash process.
  • the concentrated soak wash process also requires the presence of at least one surfactant.
  • the surfactants present are selected from the groups consisting of: anionic surfactants; cationic surfactants; zwitterionic surfactants; ampholytic nonionic surfactants; or any combinations thereof.
  • Suitable anionic surfactants are soaps and those containing sulfate or sulfonate groups.
  • Surfactants of the sulfonate type that come into consideration are (C9-C13-alkyl)benzenesulfonates and olefinsulfonates, the latter being understood to be mixtures of alkenesulfonates and hydroxyalkanesulfonates and -disulfonates, as obtained, for example, by sulfonation of C12-C18 monoolefins having a terminally or internally located double bond.
  • esters of alpha-sulfo fatty acids for example the alpha-sulfonated methyl esters of hydrogenated coconut, palm kernel or tallow fatty acids a alpha- sulfocarboxylic acids resulting from saponification of MES may be used.
  • anionic surfactants are sulfonated fatty acid glycerol esters comprising mono-, di- and tri-esters and mixtures thereof.
  • Alk(en)yl sulfates to which preference is given are the alkali metal salts and the sodium salts of sulfuric acid monoesters of C12-C18 fatty alcohols, for example from coconut fatty alcohol, tallow fatty alcohol, lauryl, myristyl, cetyl or stearyl alcohol, or of C10-C20 oxo alcohols and sulfuric acid monoesters of secondary alcohols having that chain length.
  • Suitable anionic surfactants are also alkane-2,3-diylbis(sulfates) that are prepared, for example, in accordance with US3,234,258 or US5,075,041.
  • sulfuric acid monoesters of straight-chain or branched C7-C21 alcohols ethoxylated with from 1 to 6 mole of ethylene oxide such as 2-methyl-branched C9-C11 alcohols with, on average, 3.5 mole of ethylene oxide (EO) or C12-C18 fatty alcohols with from 1 to 4 EO. Because of their high foaming characteristics, they are normally used in washing and cleaning compositions only at relatively low levels, for example at levels of from 1 % to 5% by weight.
  • Anionic surfactants may also include diesters, and/or salts of monoesters, of sulfosuccinic acid with C8-C18 fatty alcohol residues or mixtures thereof. Special preference is given to sulfosuccinates in which the fatty alcohol residues have a narrow chain length distribution. It is likewise also possible to use alk(en)yl sulfosuccinates having preferably from 8 to 18 C-atoms in the alk(en)yl chain, or salts thereof.
  • anionic surfactants that come into consideration are fatty acid derivatives of amino acids, for example of methyltaurine (taurides) and/or of methylglycine (sarcosides).
  • Further anionic surfactants that come into consideration are soaps. Saturated fatty acid soaps such as the salts of lauric acid, myristic acid, palmitic acid, stearic acid, hydrogenated erucic acid and behenic acid and soap mixtures derived from natural fatty acids, for example coconut, palm kernel or tallow fatty acids.
  • the anionic surfactants, including the soaps may be present in the form of their sodium, potassium or ammonium salts and in the form of soluble salts of organic bases such as mono-, di- or triethanolamine.
  • the anionic surfactants may be present in the form of their sodium or potassium salts.
  • the invention relates to a method, wherein the anionic surfactant is a linear alkylbenzenesulfonate; alpha-olefinsulfonate; alkyl sulfate (fatty alcohol sulfate); alcohol ethoxysulfate; secondary alkanesulfonate; alpha-sulfo fatty acid methyl ester; alkyl- or alkenylsuccinic acid; soap; or any combination thereof.
  • the anionic surfactant is a linear alkylbenzenesulfonate; alpha-olefinsulfonate; alkyl sulfate (fatty alcohol sulfate); alcohol ethoxysulfate; secondary alkanesulfonate; alpha-sulfo fatty acid methyl ester; alkyl- or alkenylsuccinic acid; soap; or any combination thereof.
  • non-ionic surfactants preferably alkoxylated, advantageously ethoxylated and/or propoxylated, especially primary alcohols having from 8 to 18 C-atoms and, on average, from 1 to 12 moles of ethylene oxide (EO) and/or from 1 to 10 moles of propylene oxide (PO) per mole of alcohol are used.
  • Special preference is given to C8-C16 alcohol alkoxylates, advantageously ethoxylated and/or propoxylated C10-C15 alcohol alkoxylates, especially C12-C14 alcohol alkoxylates, having a degree of ethoxylation between 2 and 10, or between 3 and 8, and/or a degree of propoxylation between 1 and 6, or between 1 .5 and 5.
  • the alcohol residue may be preferably linear or, especially in the 2-position, methyl-branched, or may comprise a mixture of linear and methyl-branched chains, as are usually present in oxo alcohols.
  • Special preference is given, however, to alcohol ethoxylates derived from linear alcohols of natural origin that contain from 12 to 18 C-atoms, for example coconut, palm and tallow fatty alcohol or oleyl alcohol, and on average from 2 to 8 EO per mole of alcohol.
  • the ethoxylated alcohols include, for example, C12- C14 alcohols with 3 EO or 4 EO, C9-C1 1 alcohols with 7 EO, C13-C15 alcohols with 3 EO, 5 EO, 7 EO or 8 EO, C12-18 alcohols with 3 EO, 5 EO or 7 EO, mixtures thereof, such as mixtures of C12- C14 alcohol with 3 EO and C12-C18 alcohol with 5 EO.
  • the mentioned degrees of ethoxylation and propoxylation represent statistical averages which, for a specific product, can be a whole number or a fractional number.
  • Preferred alcohol ethoxylates and propoxylates have a restricted homologue distribution (narrow range ethoxylates/propoxylates, NRE/NRP).
  • fatty alcohol ethoxylates having more than 12 EO may also be used. Examples thereof are tallow fatty alcohol ethoxylate with 14 EO, 25 EO, 30 EO or 40 EO.
  • alkoxylated amines which are ethoxylated and/or propoxylated, especially primary and secondary amines having from 1 to 18 C-atoms per alkyl chain and, on average, from 1 to 12 moles of ethylene oxide (EO) and/or from 1 to 10 moles of propylene oxide (PO) per mole of amine.
  • EO ethylene oxide
  • PO propylene oxide
  • alkyl polyglycosides of the general formula R 1 0(G) x , wherein is a primary straight-chain or methyl-branched (especially methyl-branched in the 2-position) alkyl group having from 8 to 22, preferably from 12 to 18, C- atoms and the symbol 'G' indicates a glycose (monosaccharide) unit having 5 or 6 C-atoms; preferably G is glucose.
  • the degree of oligomerisation x which indicates the average number of glycose units, will generally lie between 1 and 10; x is preferably from 1 .2 to 1.4.
  • a further class of used non-ionic surfactants which are used either as sole non-ionic surfactant or in combination with other non-ionic surfactants, comprises alkoxylated, preferably ethoxylated or ethoxylated and propoxylated fatty acid alkyl esters, having from 1 to 4 C-atoms in the alkyl chain, especially fatty acid methyl esters, as described, for example, in JP58/217598.
  • Non-ionic surfactants of the amine oxide type for example /V-(coco alkyl)-/VJv- dimethylamine oxide and /V-(tallow-alkyl)-/V,/V-bis(2-hydroxyethyl)amine oxide, and of the fatty acid alkanolamide or ethoxylated fatty acid alkanolamide type may also be suitable.
  • the invention relates to a method, wherein the non-ionic surfactant is an alcohol ethoxylate; nonylphenol ethoxylate; alkylpolyglycoside; alkyldimethylamineoxide; ethoxylated fatty acid monoethanolamide; fatty acid monoethanolamide; fatty acid (polyhydroxyalkanol)amide; /V-acyl-/V-alkyl derivatives of glucosamine (“glucamides”) ; or any combination thereof.
  • the non-ionic surfactant is an alcohol ethoxylate; nonylphenol ethoxylate; alkylpolyglycoside; alkyldimethylamineoxide; ethoxylated fatty acid monoethanolamide; fatty acid monoethanolamide; fatty acid (polyhydroxyalkanol)amide; /V-acyl-/V-alkyl derivatives of glucosamine (“glucamides”) ; or any combination thereof.
  • the invention relates to a method wherein the concentration of the at least one surfactant is from 0 to 500, from 0.00001 to 100, from 0.0001 to 50, from 0.0001 to 40, from 0.001 to 30, from 0.01 to 20, from 0.1 to 15, from 1 to 10 milligram per gram textile.
  • the invention relates to a method, wherein the concentration of the at least one surfactant is from 0 to 50, from 0.0001 to 40, from 0.001 to 30, from 0.01 to 20 from 0.1 to 10, or from 1 to 5 g per L soak solution.
  • the concentration of the at least one enzyme and the at least one surfactant are higher relative to their concentrations in the subsequent wash solution.
  • the invention relates to a method, wherein the concentration of the at least one enzyme in the wash solution is obtained by diluting the soak solution with a factor of at least 1 , 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 , 12, 13, 14, 15, 16, 17, 18, 19 or 20.
  • the invention relates to a method, wherein the concentration of the at least one surfactant in the wash solution is obtained by diluting the soak solution with a factor of at least 1 , 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 , 12, 13, 14, 15, 16, 17, 18, 19 or 20. Wash The wash period is characterized by an increased water level and is initiated by addition of water to the soaked material thereby diluting the soak solution. The weight to weight ratio of material to water is increased to a level from 1 :3.5 to 1 :6.5, from 1 :4 to 1 :5, or from 1 :4 to 1 :2.
  • the invention relates to a method, wherein agitation or other mechanical action is applied during the wash period.
  • the invention relates to a method, wherein the wash period is from 5 to 120 minutes, from 5 to 90 minutes, from 10 to 60 minutes, from 10 to 30 minutes, from 5 to 20 minutes, from 5 to 15 minutes, or from 10 to 15 minutes.
  • the concentrated two soak wash process shows in particular improved cleaning effect at reduced temperatures and accordingly, in some embodiments the invention relates to a method, wherein the temperature during the wash period is about 35°C; about 30°C; about 25°C; about 24°C; about 23°C; about 22°C; about 21°C; about 20°C; about 19°C; about 18°C; about 17°C; about 16°C; about 15°C; about 14°C; about 13°C; about 12°C; about 1 1 °C; about 10°C; about 9°C; about 8°C; about 7°C; about 6°C; or about 5°C.
  • the invention relates to a method, wherein the temperature during the wash period is below 35°C; below 30°C; below 25°C; below 24°C; below 23°C; below 22°C; below 21°C; below 20°C; below 19°C; below 18°C; below 17°C; below 16°C; below 15°C; below 14°C; below 13°C; below 12°C; below 1 1°C; below 10°C; below 9°C; below 8°C; below 7°C; below 6°C; or below 5°C.
  • the invention relates to a method wherein the temperature during the first soak period and/or the second soak period and/or the wash period are selected individually to be similar or different.
  • Next step is to let the water out and get ready for rinsing the object.
  • the rinse can be done according to the normal rinse method. If a washing device is used then the rinse program present may be used. If a concentrated two soak wash process has been applied wherein the amount of detergent has been reduced then the amount of rinse water needed for sufficient removal of detergent remnants may also be lowered.
  • the method may be applied for cleaning objects within the field of home care cleaning as well as in the field of industrial cleaning.
  • the invention is related to use of the method for cleaning fabric and/or textile.
  • the invention is related to use of the method for cleaning laundry.
  • Use of the method is furthermore an advantage when a reduction in the amount of enzymes and/or detergent is desired.
  • Example 3-III demonstrate that enzymes added to the wash process according to some embodiments of the invention result in an improved enzyme based cleaning as compared to what is obtained in a normal wash process which is apparent from the Enzyme Related Cleaning Index (ERCI).
  • ERCI Enzyme Related Cleaning Index
  • Chemicals used as buffers and substrates were commercial products of at least reagent grade.
  • surfactants were added in the form of various commercial products with chain length distributions and degrees of ethoxylation as commonly used in the art when formulating laundry detergents. Enzymes were in some cases comprised in the formulated detergent as indicated.
  • Detergent enzymes of the classes: proteases, amylases, lipases, cellulases, mannanases and pectinases were variously added, each as a commercial formulated liquid or granulated product.
  • the stained swatches used in the following examples were obtained from Center for Testmaterials BV, Vlaardingen, the Netherlands are listed below in Table I. They have been selected to addresss stain removal of the most common stains.
  • the swatches may be divided into groups according to the nature of the stain and thus their main sensitivity: Surfactant sensitive stains; enzyme specific sensitive stains like protease, lipase, cellulase, mannanase or amylase; bleach sensitive stains and tracer swatches sensitive to redeposition.
  • step 12 Press the water out by hand and transfer the wash load to a beaker with 1 L of cold tap water 13. Repeat step 12 and press the water out by hand
  • Wash performance is expressed as a delta remission value (ARem). After washing and rinsing the swatches were spread out flat and allowed to air dry at room temperature over night. Light reflectance evaluations of the swatches were done using a Macbeth Color Eye 7000 reflectance spectrophotometer with very small aperture. The measurements were made without UV in the incident light and remission at 460 nm was extracted. Measurements were made on unwashed and washed swatches. The test swatch to be measured was placed on top of another swatch of same type and color (twin swatch). Since there was only one swatch of each kind per beaker, a swatch from a replicate wash was used in this way.
  • ARem delta remission value
  • Remission values for individual swatches were calculated by subtracting the remission value of the unwashed swatch from the remission value of the washed swatch.
  • the total wash performance for each stained swatch set was calculated as the sum of individual ARem.
  • Example 1 Wash with Detergent 1
  • Detergent 1 is a liquid formulation with a pH around 8.5 and which comprises enzymes. For each wash an amount of 0.333 g detergent composition as listed below were used.
  • the 2-stage wash process provides an improved cleaning in comparison with benchmark irrespective of the absence or the presence of additional enzymes. This is apparent from the Process Related Cleaning Index (PRCI) which is 1.37 in the absence of enzymes and 1.29 in the presence of enzymes respectively.
  • PRCI Process Related Cleaning Index
  • Detergent 2 is a liquid formulation with a pH around 7.9 to 8.0 which comprises enzymes. For each wash an amount of 0.600 g detergent composition as listed below were used.
  • composition by weight
  • PEG poly(oxyethylene)
  • Table 2C ARem calculated for swatches washed in Detergent 2.
  • Detergent 3 is a liquid formulation with a pH around 8.0 to 8.1 which comprises enzymes. For each wash an amount of 0.750 g detergent composition as listed below were used.
  • composition by weight (%) of active substance specified
  • DTPA diethylenetnaminepentaacetic acid
  • PEG poly(oxyethylene)
  • Example 3-II Wash with different amounts of Detergent 3
  • Table 3-11 B Amount of Surfactant and Enzymes used
  • Table 3-11 C ARem calculated for swatches washed in different amounts of Detergent 3.
  • RWP Relative Wash Performance
  • Example 3— II I Wash with Detergent 3 and different amounts of enzymes
  • pectate Xpect 0,42 0,83 1 ,67 2,50 3,33 4, 17 5,00 lyase
  • Detergent 4 is a liquid formulation with a pH around 8.25 to 8.30 without enzymes. For each wash an amount of 0.580 g detergent composition as listed below were used. Table 4A: Detergent 4 composition
  • Detergent 5 is a liquid formulation with a pH around 10.7 to 11.1 without enzymes. For each wash an amount of 0.610 g detergent composition as listed below were used.
  • Table 5C ARem calculated for swatches washed in Detergent 5.
  • Column 5a shows the result of a normal wash at 40°C with Detergent 5.
  • Column 5b shows the result of a Normal wash at 20°C with Detergent 5.
  • Detergent 6 is a powder formulation with a pH around 11.0 to 1 1.5 without enzymes but with bleach (percarbonate). For each wash an amount of 1 .290 g detergent composition as listed below were used.
  • Table 6C ARem calculated for swatches washed in Detergent 6.
  • Detergent 7 is a liquid formulation with a pH around 8.0 to 8.2 with enzymes. For each wash an amount of 0.580 g detergent composition as listed below were used.
  • Table 7C ARem calculated for swatches washed in Detergent 7.
  • Detergent 8 is a liquid formulation with a pH around 9.1 to 9.2 with enzymes. For each wash an amount of 0.570 g detergent composition as listed below were used.
  • Detergent 9 is a liquid formulation with a pH around 10.6 to 10.8 without enzymes and a low level of surfactant. For each wash an amount of 0.580 g detergent composition as listed below were used.
  • Detergent 10 is a liquid formulation with a pH around 8.1 to 8.3 without enzymes and a low level of surfactant. For each wash an amount of 0.560 g detergent composition as listed below were used.
  • Detergent 1 1 is a liquid formulation with a pH around 1 1.2 to 1 1.4 without enzymes and a low level of surfactant. For each wash an amount of 0.580 g detergent composition as listed below were used.
  • Table 11 C ARem calculated for swatches washed in Detergent 11.
  • Detergent 12 is a powder formulation with a pH around 10.7 without enzymes. For each small scale wash an amount of 0.580 g and for each large scale wash an amount of 65 g detergent composition as listed below were used.
  • Table 12Aa Detergent 12 composition for small scale wash
  • Ballast 6 cotton T-shirts. 8 shirts and 1 t-towel of a total weight of 2.6 kg was used as ballast fabric. Ballast was pre-washed with 5 g/L Liquid "Neutral” a commercial detergent without enzymes using the wash program: 40°C "koge/kul0rt” in tap water in an EU front load machine. 100 mL 5% acetic acid was added to the rinse. The second rinse was performed in tap water using the program "STIVELSE" after which the ballast was tumble dried. After test wash the ballast was inactivated in tap water at 95°C using an EU front load machine.
  • Stained swatches During wash two of each soiled swatches were attached to two t-towel. After wash all swatches were removed from the T-towel and placed on filter paper and dried over night in darkness. The swatches were evaluated and delta remission values calculated as described above.
  • Enzymes The following enzymes: Amylase, Celluclean, Lipex, Savinase were used at the concentrations given in table II. Celluclean was added with the detergent and stirred for 10 minutes. The liquid enzymes were added to the soak or wash volume just before use.
  • Detergent 12 was used at a dosage of 5 g/L wash solution corresponding to 65 g per wash.
  • Water hardness to 15°dH was adjusted after heating of water to the desired temperature by addition of 2.5 ml/L of a Ca/Mg 4: 1 6000°dH/L stock solution and 7.5 ml/L of a 0.535 M Sodium hydrogencarbonate stock solution.
  • Front load washing device The Miele Profitronic PW 61601 is not designed for wash with low water volumes such as the concentrated soak wash. Suitable wash programs were designed using the Profitronic M 1 .1.214 software. Programs for a normal wash process, concentrated soak wash, as well as programs for Rinse 1 and Rinse 2 are outlined in the table below. The two rinse programs using cold tap water (22°dH) were applied in all wash processes.
  • Block data Area 2 Block 1 Block data Area 2 Block 1
  • Main wash Block data Area 2 Block 1
  • Main wash Block data Area 2 Block 1 , Main wash:
  • Hysteresis Normal
  • Dispensing type No 1 1) Dispensing type: No 1 2) Dispensing type: No 1 1) Dispensing type: No
  • Level stop 1 No 15) Level stop 1 : No
  • Drain path 1 Drainage 28) Drain path 1 : Drainage
  • Drain level 0 mm wc 29) Drain level: 0 mm wc
  • Drain path 2 Drainage 31
  • Drain path 2 Drainage
  • Block repetition Blocks:: No Programmes:: 34) Block repetition: Blocks:: No Programmes:: 34) Block repetition: Blocks:: No Programmes::
  • Block end signal No 35) Block end signal: No 35) Block end signal: No
  • Block activation: Permanent Block activation: Permanent
  • Hysteresis Normal
  • Dispensing type No 1 1) Dispensing type: No 1 2) Dispensing type: No 1 1) Dispensing type: No
  • Level stop 1 Yes 15) Level stop 1 : Yes
  • Drain path 1 Drainage 28) Drain path 1 : Drainage
  • Drain level 0 mm wc 29) Drain level: 0 mm wc
  • Drain path 2 Drainage 31
  • Drain path 2 Drainage
  • Block repetition Blocks:: No Programmes:: Spin phase 1 : 500 U/min 02:00 min:s Rhythm: No No
  • Block end signal No Spin phase 2: Normal 00:30 min:s Rhythm: Washing Gentle
  • Block repetition Blocks: No Programmes: No
  • Normal wash process Place the dry ballast fabric and the two t-towels with soiled test swatches into Miele Profitronic PW6101. The temperature of the water is adjusted to 20°C before use. Water hardness solutions were added to a beaker containing 4000 ml 20°C de- ionized water to which detergent 12 was added and agitation applied for 10 minutes. If enzymes were needed Celluclean was added with the detergent and the other enzymes were added to the beaker just before pouring the wash solution into Miele Profitronic PW6101. Make 2 x 4500 ml with 20°C de-ionized water with a water hardness of 15°d H . If a 40°C wash is set up then the temperature of the water should be approximately 55°C. Add all 3 beakers of wash solution into the detergent dispenser and start Program 1.
  • 2-stage wash process (large scale): The temperature of the water is adjusted to 20°C before use. Water hardness solutions were added to a beaker containing 4000 ml 20°C de-ionized water to which detergent 12 was added and agitation applied for 10 minutes. If enzymes were needed Celluclean was added with the detergent and the other enzymes were added to the beaker just before pouring the wash solution into Miele Profitronic PW6101.
  • Soak Split the dry ballast fabric into three parts. Place one part in a 100 L clear plastic bag and place the first t-towel with soiled test swatches on top and pour over with 2 L soak solution. Add the second part of ballast fabric on top and place the second t-towel with soiled test swatches thereon and pour over with 1 L soak solution. Add the third part of ballast fabric and wet with the last 1 L soak solution. Close the bag securely with an electrician plastic strip leaving some air in the bag for the load to be able to mix during soak. Place the bag in Miele Profitronic PW6101 and start program 2. After 9 minutes the program is stopped.
  • Table 12C ARem calculated for swatches washed in Detergent 12.
  • Total wash performance of the 2-stage wash process with enzymes at 20°C (column e) is higher relative to a normal wash at 40°C (column a).
  • the 2-stage wash process provides an improved cleaning in comparison with benchmark irrespective of the absence or the presence of additional enzymes. This is apparent from the Process Related Cleaning Index (PRCI) which is 1 .15 in the absence of enzymes and 1.1 1 in the presence of enzymes respectively.
  • PRCI Process Related Cleaning Index
  • Detergent 13A and Detergent 13B are powder formulations with a pH around 9.8. These detergents are identical except for the presence of protease in detergent 13A. The enzymes have been inactivated by treatment in a microwave oven. For each wash an amount of 50 g detergent composition as listed below were used.
  • composition by weight
  • Top loader washing device The Royalstar XPB60-801 S top loading semi-Automatic Washing Machine has two wash drums. One is in bigger size for wash process, and the other is in smaller size for spinning. Three control knobs can be found on front panel. Two of the knobs are designed to control wash time and spin time respectively. The middle one on is set as a switch between Heavy duty, Normal wash and Drain options. Thus, the operation of this type of washing machine is quite simple. Water levels (0 to 65 Litres), Wash time (0 to 15 minutes), Soaking time and Spin time can be adjusted manually in accordance with different wash conditions. The engine of agitator inside can even be started without water input.
  • the wash process 24 grams of detergent 13 for the soak solution and 26 grams for the wash solution were placed in separate beakers.
  • the enzymes contained in the detergent were deactivated by heating the powder in a microwave oven and cooled to room temperature prior to use. 3 L water was added to each beaker.
  • Ballast and swatches were placed in a big plastic bag, and the 3-Liter soak solution was poured into the bag which was sealed and packed tightly.
  • the plastic bag was placed in the wash drum without water and 5-minutes agitation was applied. After the 3-minute holding period the bag was opened and water was added to the wash drum to a total of 38 Liters. Add the wash solution to wash drum and turn on the agitation for 10-minutes washing. This was followed by two rinses (5 minutes, 38 Liters)) and a final spinning (5 minutes).
  • the test swatches were removed from the tea towel and place on filter paper for drying in darkness at room temperature over night. The swatches were evaluated as described above.
  • Table 13C ARem calculated for swatches washed in Detergent 13A or 13B.
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DE102013226835A1 (de) * 2013-12-20 2015-06-25 Henkel Ag & Co. Kgaa Wasch- oder Reinigungsmittel mit reduziertem Tensidgehalt
EP3105321A1 (de) * 2014-02-11 2016-12-21 Novozymes A/S Reinigungsmittelzusammensetzung und verwendung der reinigungsmittelzusammensetzung
WO2016066369A1 (en) * 2014-10-29 2016-05-06 Unilever Plc Reduction of colour damage during the laundry process
CN111434834B (zh) * 2018-12-26 2023-03-28 青岛海尔洗衣机有限公司 一种洗衣机的控制方法及洗衣机
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ZA201300109B (en) 2013-09-25
JP2013541356A (ja) 2013-11-14
RU2013114300A (ru) 2014-10-10
UY33579A (es) 2012-03-30
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MX2013002248A (es) 2013-05-09

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